| http://purl.uniprot.org/citations/10551873 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10551873 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10551873 | http://www.w3.org/2000/01/rdf-schema#comment | "Membrane type (MT) matrix metalloproteinases (MMPs) are recently recognized members of the family of Zn(2+)- and Ca(2+)-dependent MMPs. To investigate the proteolytic capabilities of human MT4-MMP (i.e. MMP-17), we have cloned DNA encoding its catalytic domain (CD) from a breast carcinoma cDNA library. Human membrane type 4 MMP CD (MT4-MMPCD) protein, expressed as inclusion bodies in Escherichia coli, was purified to homogeneity and refolded in the presence of Zn(2+) and Ca(2+). While MT4-MMPCD cleaved synthetic MMP substrates Ac-PLG-[2-mercapto-4-methylpentanoyl]-LG-OEt and Mca-PLGL-Dpa-AR-NH(2) with modest efficiency, it catalyzed with much higher efficiency the hydrolysis of a pro-tumor necrosis factor-alpha converting enzyme synthetic substrate, Mca-PLAQAV-Dpa-RSSSR-NH(2). Catalytic efficiency with the pro-tumor necrosis factor-alpha converting enzyme substrate was maximal at pH 7.4 and was modulated by three ionizable enzyme groups (pK(a3) = 6.2, pK(a2) = 8.3, and pK(a1) = 10.6). MT4-MMPCD cleaved gelatin but was inactive toward type I collagen, type IV collagen, fibronectin, and laminin. Like all known MT-MMPs, MT4-MMPCD was also able to activate 72-kDa progelatinase A to its 68-kDa form. EDTA, 1,10-phenanthroline, reference hydroxamic acid MMP inhibitors, tissue inhibitor of metalloproteinases-1, and tissue inhibitor of metalloproteinases-2 all potently blocked MT4-MMPCD enzymatic activity. MT4-MMP is, therefore, a competent Zn(2+)-dependent MMP with unique specificity among synthetic substrates and the capability to both degrade gelatin and activate progelatinase A."xsd:string |
| http://purl.uniprot.org/citations/10551873 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.274.46.33043"xsd:string |
| http://purl.uniprot.org/citations/10551873 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.274.46.33043"xsd:string |
| http://purl.uniprot.org/citations/10551873 | http://purl.uniprot.org/core/author | "Wang Y."xsd:string |
| http://purl.uniprot.org/citations/10551873 | http://purl.uniprot.org/core/author | "Wang Y."xsd:string |
| http://purl.uniprot.org/citations/10551873 | http://purl.uniprot.org/core/author | "Johnson A.R."xsd:string |
| http://purl.uniprot.org/citations/10551873 | http://purl.uniprot.org/core/author | "Johnson A.R."xsd:string |
| http://purl.uniprot.org/citations/10551873 | http://purl.uniprot.org/core/author | "Ye Q.-Z."xsd:string |
| http://purl.uniprot.org/citations/10551873 | http://purl.uniprot.org/core/author | "Ye Q.-Z."xsd:string |
| http://purl.uniprot.org/citations/10551873 | http://purl.uniprot.org/core/author | "Dyer R.D."xsd:string |
| http://purl.uniprot.org/citations/10551873 | http://purl.uniprot.org/core/author | "Dyer R.D."xsd:string |
| http://purl.uniprot.org/citations/10551873 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10551873 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10551873 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/10551873 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/10551873 | http://purl.uniprot.org/core/pages | "33043-33049"xsd:string |
| http://purl.uniprot.org/citations/10551873 | http://purl.uniprot.org/core/pages | "33043-33049"xsd:string |
| http://purl.uniprot.org/citations/10551873 | http://purl.uniprot.org/core/title | "Catalytic activities and substrate specificity of the human membrane type 4 matrix metalloproteinase catalytic domain."xsd:string |
| http://purl.uniprot.org/citations/10551873 | http://purl.uniprot.org/core/title | "Catalytic activities and substrate specificity of the human membrane type 4 matrix metalloproteinase catalytic domain."xsd:string |
| http://purl.uniprot.org/citations/10551873 | http://purl.uniprot.org/core/volume | "274"xsd:string |
| http://purl.uniprot.org/citations/10551873 | http://purl.uniprot.org/core/volume | "274"xsd:string |
| http://purl.uniprot.org/citations/10551873 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10551873 |
| http://purl.uniprot.org/citations/10551873 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10551873 |